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The primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence.
The complete primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase has been determined by automated Edman degradation and carboxypeptidase digestionof the intact alpha chain and of peptides derived from trypsin (N.A. Kohlmiller and J.B. Howard (1979) J. Biol. Chem. 254, 7302-7308) and Staphylococcus aureus protease digestion, and from hydroxylamine and dilute acid cleavage. The alpha chain was found to consist of 200 residues in the following sequence from the NH2-terminal end: (formula: see text).
PMID: 465136 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes.
Frazee RW, Livingston DM, LaPorte DC, Lipscomb JD.
J Bacteriol. 1993 Oct; 175(19):6194-202.
[J Bacteriol. 1993]
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Amino acid sequence requirements in the epitope recognized by the alpha-tubulin-specific rat monoclonal antibody YL 1/2.
Wehland J, Schröder HC, Weber K.
EMBO J. 1984 Jun; 3(6):1295-300.
[EMBO J. 1984]
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Genetic organization and sequence of the Pseudomonas cepacia genes for the alpha and beta subunits of protocatechuate 3,4-dioxygenase.
Zylstra GJ, Olsen RH, Ballou DP.
J Bacteriol. 1989 Nov; 171(11):5915-21.
[J Bacteriol. 1989]
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